P0ABR9 (MHPB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
EC=1.13.11.16

Alternative name(s):
3-carboxyethylcatechol 2,3-dioxygenase

Gene names

Name:	mhpB
Ordered Locus Names:	b0348, JW0339

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	314 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. Ref.6
Catalytic activity	3-(2,3-dihydroxyphenyl)propanoate + O2 = (2Z,4E)-2-hydroxy-6-oxonona-2,4-diene-1,9-dioate. HAMAP-Rule MF_01653 (2E)-3-(2,3-dihydroxyphenyl)prop-2-enoate + O2 = (2Z,4E,7E)-2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioate. HAMAP-Rule MF_01653
Pathway	Aromatic compound metabolism; 3-phenylpropanoate degradation. HAMAP-Rule MF_01653
Subunit structure	Homotetramer. Ref.6
Sequence similarities	Belongs to the LigB/MhpB extradiol dioxygenase family.
Biophysicochemical properties	Kinetic parameters: KM=26 µM for 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8) Ref.1 Ref.6 KM=36 µM for 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8) KM=37 µM for methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8) KM=90 µM for 3-methylcatechol (at 20 degrees Celsius and pH 8) KM=94 µM for 3-phenethylcatechol (at 20 degrees Celsius and pH 8) KM=154 µM for 3-propylcatechol (at 20 degrees Celsius and pH 8) KM=185 µM for 3-ethylcatechol (at 20 degrees Celsius and pH 8) KM=300 µM for 2,3-dihydroxyphenoxyacetic acid (at 20 degrees Celsius and pH 8) KM=700 µM for catechol (at 20 degrees Celsius and pH 8)

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	3-(3-hydroxy)phenylpropionate catabolic process Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc 3-phenylpropionate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phenylpropanoid catabolic process Inferred from mutant phenotype PubMed 3531186. Source: EcoCyc
Molecular_function	3-carboxyethylcatechol 2,3-dioxygenase activity Inferred from direct assay Ref.6. Source: EcoCyc ferrous iron binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 314	314	2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase HAMAP-Rule MF_01653		PRO_0000085103
Sites
	Active site	115	1	Proton donor
	Active site	179	1	Proton acceptor
Experimental info
	Mutagenesis	114	1	D → A: Complete loss of extradiol cleavage activity. Ref.7
	Mutagenesis	114	1	D → N: Low level of catalytic activity, 600-fold lower than the wild-type enzyme. More than 8000-fold decrease in affinity. Ref.7
	Mutagenesis	115	1	H → A: Complete loss of extradiol cleavage activity. Ref.7
	Mutagenesis	115	1	H → Q: Complete loss of activity. Ref.7
	Mutagenesis	115	1	H → Y: Complete loss of activity. Ref.7
	Mutagenesis	179	1	H → A: Complete loss of activity. Ref.7
	Mutagenesis	179	1	H → Q: Complete loss of activity. Ref.7
	Mutagenesis	179	1	H → Y: Complete loss of activity. Ref.7
	Mutagenesis	181	1	P → A: More than 2-fold decrease in catalytic activity and 100-fold decrease in affinity. Ref.7
	Mutagenesis	181	1	P → H: More than 60-fold decrease in catalytic activity and affinity. Ref.7
	Sequence conflict	138 – 140	3	ING → NKA in BAA13053. Ref.1
	Sequence conflict	152	1	R → H in BAA13053. Ref.1
	Sequence conflict	157	1	A → T in BAA13053. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0ABR9 [UniParc]. Last modified November 8, 2005. Version 1. Checksum: E1D5A8574E5DFE05	FASTA	314	34,196
	10 20 30 40 50 60 MHAYLHCLSH SPLVGYVDPA QEVLDEVNGV IASARERIAA FSPELVVLFA PDHYNGFFYD 70 80 90 100 110 120 VMPPFCLGVG ATAIGDFGSA AGELPVPVEL AEACAHAVMK SGIDLAVSYC MQVDHGFAQP 130 140 150 160 170 180 LEFLLGGLDK VPVLPVFING VATPLPGFQR TRMLGEAIGR FTSTLNKRVL FLGSGGLSHQ 190 200 210 220 230 240 PPVPELAKAD AHMRDRLLGS GKDLPASERE LRQQRVISAA EKFVEDQRTL HPLNPIWDNQ 250 260 270 280 290 300 FMTLLEQGRI QELDAVSNEE LSAIAGKSTH EIKTWVAAFA AISAFGNWRS EGRYYRPIPE 310 WIAGFGSLSA RTEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catechol dioxygenases from Escherichia coli (MhpB) and Alcaligenes eutrophus (MpcI): sequence analysis and biochemical properties of a third family of extradiol dioxygenases." Spence E.L., Kawamukai M., Sanvoisin J., Braven H., Bugg T.D.H. J. Bacteriol. 178:5249-5256(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOPHYSICOCHEMICAL PROPERTIES. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." Ferrandez A., Garcia J.L., Diaz E. J. Bacteriol. 179:2573-2581(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / CS520.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Overproduction, purification and properties of 2,3-dihydroxyphenylpropionate 1,2-dioxygenase from Escherichia coli." Bugg T.D.H. Biochim. Biophys. Acta 1202:258-264(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15, SUBUNIT, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[7]	"Acid-base catalysis in the extradiol catechol dioxygenase reaction mechanism: site-directed mutagenesis of His-115 and His-179 in Escherichia coli 2,3-dihydroxyphenylpropionate 1,2-dioxygenase (MhpB)." Mendel S., Arndt A., Bugg T.D.H. Biochemistry 43:13390-13396(2004) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-114; HIS-115; HIS-179 AND PRO-181, REACTION MECHANISM.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D86239 Genomic DNA. Translation: BAA13053.1. Y09555 Genomic DNA. Translation: CAA70748.1. U73857 Genomic DNA. Translation: AAB18072.1. U00096 Genomic DNA. Translation: AAC73451.1. AP009048 Genomic DNA. Translation: BAE76130.1.
PIR	D64762.
RefSeq	NP_414882.1. NC_000913.2. YP_488642.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0ABR9.
SMR	P0ABR9. Positions 43-204.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0ABR9. 5 interactions.
STRING	511145.b0348.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73451; AAC73451; b0348. BAE76130; BAE76130; BAE76130.
GeneID	12931736. 945047.
KEGG	ecj:Y75_p0337. eco:b0348.
PATRIC	32115829. VBIEscCol129921_0356.
Organism-specific databases
EchoBASE	EB4167.
EcoGene	EG20274. mhpB.
Phylogenomic databases
eggNOG	NOG08474.
HOGENOM	HOG000069851.
KO	K05713.
OMA	AHEIRTW.
ProtClustDB	PRK13370.
Enzyme and pathway databases
BioCyc	EcoCyc:DHPDIOXYGEN-MONOMER. ECOL316407:JW0339-MONOMER. MetaCyc:DHPDIOXYGEN-MONOMER.
BRENDA	1.13.11.16. 2026.
SABIO-RK	P0ABR9.
UniPathway	UPA00714.
Gene expression databases
Genevestigator	P0ABR9.
Family and domain databases
Gene3D	3.40.830.10. 2 hits.
HAMAP	MF_01653. MhpB.
InterPro	IPR023789. DHPP/DHXA_dioxygenase. IPR004183. Xdiol_dOase_suB. [Graphical view]
Pfam	PF02900. LigB. 1 hit. [Graphical view]
SUPFAM	SSF53213. Xdiol_dOase_3B. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MHPB_ECOLI

Accession

Primary (citable) accession number: P0ABR9
Secondary accession number(s): P54711 , P77048, P77461, Q2MC76

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
Last sequence update:	November 8, 2005
Last modified:	May 1, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program